Complete kinetic and thermodynamic characterization of the unisite catalytic pathway of Escherichia coli F1-ATPase. Comparison with mitochondrial F1-ATPase and application to the study of mutant enzymes.-Reference-Cited by-同舟云学术

Complete kinetic and thermodynamic characterization of the unisite catalytic pathway of Escherichia coli F1-ATPase. Comparison with mitochondrial F1-ATPase and application to the study of mutant enzymes.

Published:1988-12 Issue:36 Volume:263 Page:19640-19648
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Al-Shawi M K,Senior A E

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference39 articles.

1. Temperature dependence and mechanism of local anesthetic effects on mitochondrial adenosinetriphosphatase

2. Directed mutagenesis of the strongly conserved aspartate 242 in the beta-subunit of Escherichia coli proton-ATPase.

3. Evolution of enzyme function and the development of catalytic efficiency

4. The unusual enzymology of ATP synthase

5. The Mechanism and Regulation of ATP Synthesis by F1-ATPases

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